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Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-A resolution.

ABSTRACT: The intracellular protease from Pyrococcus horikoshii (PH1704) and PfpI from Pyrococcus furiosus are members of a class of intracellular proteases that have no sequence homology to any other known protease family. We report the crystal structure of PH1704 at 2.0-A resolution. The protease is tentatively identified as a cysteine protease based on the presence of cysteine (residue 100) in a nucleophile elbow motif. In the crystal, PH1704 forms a hexameric ring structure, and the active sites are formed at the interfaces between three pairs of monomers.

SUBMITTER: Du X

PROVIDER: S-EPMC18874 | biostudies-literature | 2000 Dec

REPOSITORIES: biostudies-literature

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Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-A resolution.

Du X X Choi I G IG Kim R R Wang W W Jancarik J J Yokota H H Kim S H SH

Proceedings of the National Academy of Sciences of the United States of America 20001201 26

The intracellular protease from Pyrococcus horikoshii (PH1704) and PfpI from Pyrococcus furiosus are members of a class of intracellular proteases that have no sequence homology to any other known protease family. We report the crystal structure of PH1704 at 2.0-A resolution. The protease is tentatively identified as a cysteine protease based on the presence of cysteine (residue 100) in a nucleophile elbow motif. In the crystal, PH1704 forms a hexameric ring structure, and the active sites are f ...[more]

PMID: 11114201

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